1W8M: Enzymatic and Structural Characterisation of NON Peptide Ligand Cyclophilin Complexes

Piperidine ligands are described that provide the first examples of non-peptidic ligand structures for the cyclophilin family of proteins. Crystal structures of two ligand complexes are compared with the unliganded protein and show ligand-induced changes in side-chain conformation and water binding. A peptidylprolyl cis-trans-isomerase assay showed the dissociation constants of the two ligands to be 320 and 25 mM. This study also provides the first published data for both enzymatic activity and three-dimensional structure for any protein-ligand complex that binds with a high-millimolar dissociation constant. The structures may be of relevance in the field of drug design, as they suggest starting points for the design of larger tighter-binding analogues.
PDB ID: 1W8MDownload
MMDB ID: 29736
PDB Deposition Date: 2004/9/24
Updated in MMDB: 2007/11
Experimental Method:
x-ray diffraction
Resolution: 1.65  Å
Source Organism:
Similar Structures:
Biological Unit for 1W8M: monomeric; determined by author and by software (PQS)
Molecular Components in 1W8M
Label Count Molecule
Protein (1 molecule)
Peptidyl-prolyl Cis-trans Isomerase a(Gene symbol: PPIA)
Molecule annotation
Chemical (1 molecule)
* Click molecule labels to explore molecular sequence information.

Citing MMDB